Therapy through chaperones: Sense or antisense? Cystic fibrosis as a model disease

Journal of Inherited Metabolic Disease

Volumn 29, Issue 2-3, 2006, Pages 477-487

  Amaral, Margarida D ^a,b  

^a UNIVERSITY OF LISBON   (Portugal)

^b NATIONAL INSTITUTE OF HEALTH DR RICARDO JORGE   (Portugal)

Author keywords

[No Author keywords available]

Indexed keywords

BENZO[C]QUINOLIZINE DERIVATIVE; CHAPERONE; GENE PRODUCT; MUTANT PROTEIN; QUINOLIZINE DERIVATIVE; TRANSMEMBRANE CONDUCTANCE REGULATOR; UNCLASSIFIED DRUG;

ARTICLE; CYSTIC FIBROSIS; DRUG MECHANISM; ENDOPLASMIC RETICULUM; GENE MUTATION; GENETIC DISORDER; HUMAN; MOLECULAR DYNAMICS; NONHUMAN; PROTEIN ANALYSIS; PROTEIN DEGRADATION; PROTEIN FOLDING; PROTEIN FUNCTION; QUALITY CONTROL; RNA INTERFERENCE; WILD TYPE;

ANIMALS; CYSTIC FIBROSIS; CYSTIC FIBROSIS TRANSMEMBRANE CONDUCTANCE REGULATOR; HUMANS; MOLECULAR CHAPERONES; MUTATION; PROTEIN CONFORMATION; PROTEIN FOLDING;

EID: 33745091537     PISSN: 01418955     EISSN: 15732665     Source Type: Journal    
DOI: 10.1007/s10545-006-0251-x     Document Type: Article

References (76)

1. Alberti S, Bohse K, Arndt V, Schmitz A, Hohfeld J (2004) The co-chaperone HspBP1 inhibits the CHIP ubiquitin ligase and stimulates the maturation of the cystic fibrosis transmembrane conductance regulator. Mol Biol Cell 15: 4003-4010.
2. Amaral MD (2004) CFTR and chaperones: Processing and degradation. J Mol Neurosci 23: 41-48.
3. Amaral MD (2005) Processing of CFTR: Traversing the cellular maze-how much CFTR needs to go through to avoid cystic fibrosis? Pediatr Pulmonol 39: 479-491.
4. Arndt V, Daniel C, Nastainczyk W, Alberti S, Hohfeld J (2005) BAG-2 acts as an inhibitor of the chaperone-associated ubiquitin ligase CHIP. Mol Biol Cell 16: 5891-5900.
5. Barral JM, Broadley SA, Schaffar G, Hartl FU (2004) Roles of molecular chaperones in protein misfolding diseases. Semin Cell Dev Biol 15: 17-29.
6. Benharouga M, Sharma M, Lukacs GL (2002) CFTR folding and maturation in cells. Methods Mol Med 70: 229-243.
7. Bernier V, Lagace M, Bichet DG, Bouvier M (2004) Pharmacological chaperones: Potential treatment for conformational diseases. Trends Endocrinol Metab 15: 222-228.
8. Brown CR, Hong-Brown LQ, Welch WJ (1997) Correcting temperature-sensitive protein folding defects. J Clin Invest 99: 1432-1444.
9. Buchner J (1999) Hsp90 & Co.-a holding for folding. Trends Biochem Sci 24: 136-141.
10. Bukau B, Horwich AL (1998) The Hsp70 and Hsp60 chaperone machines. Cell 92: 351-366.
11. Bykov VJ, Selivanova G, Wiman KG (2003) Small molecules that reactivate mutant p53. Eur J Cancer 39: 1828-1834.
12. Cabral CM, Liu Y, Sifers RN (2001) Dissecting glycoprotein quality control in the secretory pathway. Trends Biochem Sci 26: 619-624.
13. Caplan AJ (1999) Hsp90's secrets unfold: New insights from structural and functional studies. Trends Cell Biol 9: 262-268.
14. Catelli MG, Binart N, Jung-Testas I, et al (1985) The common 90-kd protein component of non-transformed '8S' steroid receptors is a heat-shock protein. EMBO J 4: 3131-3135.
15. Cheng SH, Gregory RJ, Marshall J, et al (1990) Defective intracellular transport and processing of CFTR is the molecular basis of most cystic fibrosis. Cell 63: 827-834.
16. Cohen FE, Kelly JW (2003) Therapeutic approaches to protein-misfolding diseases. Nature 426: 905-909.
17. Collins FS (1992) Cystic fibrosis: Molecular biology and therapeutic implications. Science 256: 774-779.
18. Denning GM, Anderson MP, Amara JF, Marshall J, Smith AE, Welsh MJ (1992) Processing of mutant cystic fibrosis transmembrane conductance regulator is temperature-sensitive. Nature 358: 761-764.
19. Desnick RJ (2004) Enzyme replacement and enhancement therapies for lysosomal diseases. J Inherit Metab Dis 27: 385-410.
20. Dorner AJ, Krane MG, Kaufman RJ (1988) Reduction of endogenous GRP78 levels improves secretion of a heterologous protein in CHO cells. Mol Cell Biol 8: 4063-4070.
21. Ellis RJ, van der Vies SM, Hemmingsen SM (1989) The molecular chaperone concept. Biochem Soc Symp 55: 145-153.
22. Farinha CM, Amaral MD (2005) Most F508del-CFTR is targeted to degradation at an early folding checkpoint and independently of calnexin. Mol Cell Biol 25: 5242-5252.
23. Farinha CM, Nogueira P, Mendes F, Penque D, Amaral MD (2002) The human DnaJ homologue (Hdj)-1/heat-shock protein (Hsp) 40 co-chaperone is required for the in vivo stabilization of the cystic fibrosis transmembrane conductance regulator by Hsp70. Biochem J 366: 797-806.
24. Frydman J (2001) Folding of newly translated proteins in vivo: The role of molecular chaperones. Annu Rev Biochem 70: 603-647.
25. Frydman J, Hohfeld J (1997) Chaperones get in touch: The Hip-Hop connection. Trends Biochem Sci 22: 87-92.
26. Graner MW, Bigner DD (2005) Chaperone proteins and brain tumors: potential targets and possible therapeutics. Neuro-oncol 7: 260-278.
27. Green DR, Beere HM (2001) Apoptosis. Mostly dead. Nature 412: 133-135.
28. Hartl FU (1996) Molecular chaperones in cellular protein folding. Nature 381: 571-579.
29. Hartl FU, Hayer-Hartl M (2002) Molecular chaperones in the cytosol: From nascent chain to folded protein. Science 295: 1852-1858.
30. Hartl FU, Martin J (1995) Molecular chaperones in cellular protein folding. Curr Opin Struct Biol 5: 92-102.
31. Helenius A, Aebi M (2004) Roles of N-linked glycans in the endoplasmic reticulum. Annu Rev Biochem 73: 1019-1049.
32. Hendrick JP, Hartl FU (1993) Molecular chaperone functions of heat-shock proteins. Annu Rev Biochem 62: 349-384.
33. Hightower LE (1980) Cultured animal cells exposed to amino acid analogues or puromycin rapidly synthesize several polypeptides. J Cell Physiol 102: 407-427.
34. Hightower LE (1991) Heat shock, stress proteins, chaperones, and proteotoxicity. Cell 66: 191-197.
35. Hohfeld J, Cyr DM, Patterson C (2001) From the cradle to the grave: molecular chaperones that may choose between folding and degradation. EMBO Rep 2: 885-890.
36. Jensen TJ, Loo MA, Pind S, Williams DB, Goldberg AL, Riordan JR (1995) Multiple proteolytic systems, including the proteasome, contribute to CFTR processing. Cell 83: 129-135.
37. Jones GW, Tuite MF (2005) Chaperoning prions: The cellular machinery for propagating an infectious protein? Bioessays 27: 823-832.
38. Klein I, Sarkadi B, Varadi A (1999) An inventory of the human ABC proteins. Biochim Biophys Acta 1461: 237-262.
39. Lenk U, Yu H, Walter J, Gelman MS, Hartmann E, Kopito RR, Sommer T (2002) A role for mammalian Ubc 6 homologues in ER-associated degradation. J Cell Sci 115: 3007-3014.
40. Loo MA, Jensen TJ, Cui L, Hou Y, Chang XB, Riordan JR (1998) Perturbation of Hsp90 interaction with nascent CFTR prevents its maturation and accelerates its degradation by the proteasome. EMBO J 17: 6879-6887.
41. Lukacs GL, Mohamed A, Kartner N, Chang XB, Riordan JR, Grinstein S (1994) Conformational maturation of CFTR but not its mutant counterpart (delta F508) occurs in the endoplasmic reticulum and requires ATP. EMBO J 13: 6076-6086.
42. McClellan AJ, Frydman J (2001) Molecular chaperones and the art of recognizing a lost cause. Nat Cell Biol 3: E51-E53.
43. McCracken AA, Brodsky JL (2003) Evolving questions and paradigm shifts in endoplasmic-reticulum-associated degradation (ERAD). Bioessays 25: 868-877.
44. Meacham GC, Lu Z, King S, Sorscher E, Tousson A, Cyr DM (1999) The Hdj-2/ Hsc70 chaperone pair facilitates early steps in CFTR biogenesis. EMBO J 18: 1492-1505.
45. Meacham GC, Patterson C, Zhang W, Younger JM, Cyr DM (2001) The Hsc70 co-chaperone CHIP targets immature CFTR for proteasomal degradation. Nat Cell Biol 3: 100-105.
46. Mendes F, Farinha CM, Roxo RM, et al (2004) Antibodies for CFTR studies. J Cyst Fibros 3 (Supplement 2):69-72.
47. Mendes F, Wakefield J, Bachhuber T, et al (2005) Establishment and characterization of a novel polarized MDCK epithelial cellular model for CFTR studies. Cell Physiol Biochem 16: 281-290.
48. Morello JP, Salahpour A, Laperriere A, et al (2000) Pharmacological chaperones rescue cell-surface expression and function of misfolded V2 vasopressin receptor mutants. J Clin Invest 105: 887-895.
49. Muchowski PJ, Wacker JL (2005) Modulation of neurodegeneration by molecular chaperones. Nat Rev Neurosci 6: 11-22.
50. Oda Y, Hosokawa N, Wada I, Nagata K (2003) EDEM as an acceptor of terminallymisfolded glycoproteins released from calnexin. Science 299: 1394-1397.
51. Pandey P, Saleh A, Nakazawa A, et al (2000) Negative regulation of cytochrome c -mediated oligomerization of Apaf-1 and activation of procaspase-9 by heat shock protein 90. EMBO J 19: 4310-4322.
52. Pardue ML (1988) The heat shock response in biology and human disease: A meeting review. Genes Dev 2: 783-785.
53. Pind S, Riordan JR, Williams DB (1994) Participation of the endoplasmic reticulum chaperone calnexin (p88, IP90) in the biogenesis of the cystic fibrosis transmembrane conductance regulator. J Biol Chem 269: 12784-12788.
54. Pratt WB, Toft DO (2003) Regulation of signaling protein function and trafficking by the hsp90/hsp70-based chaperone machinery. Exp Biol Med 228: 111-133.
55. Prodromou C, Roe SM, O'Brien R, Ladbury JE, Piper PW, Pearl LH (1997) Identification and structural characterization of the ATP/ADP-binding site in the Hsp90 molecular chaperone. Cell 90: 65-75.
56. Qu BH, Thomas PJ (1996) Alteration of the cystic fibrosis transmembrane conductance regulator folding pathway. J Biol Chem 271: 7261-7264.
57. Riordan JR (1993) The cystic fibrosis transmembrane conductance regulator. Annu Rev Physiol 55: 609-630.
58. Riordan JR (1999) Cystic fibrosis as a disease of misprocessing of the cystic fibrosis transmembrane conductance regulator glycoprotein. Am J Hum Genet 64: 1499-1504.
59. Rowe SM, Miller S, Sorscher EJ (2005) Cystic fibrosis. N Engl J Med 352: 1992-2001.
60. Sato S, Ward CL, Krouse ME, Wine JJ, Kopito RR (1996) Glycerol reverses the misfolding phenotype of the most common cystic fibrosis mutation. J Biol Chem 271: 635-638.
61. Tatzelt J, Prusiner SB, Welch WJ (1996) Chemical chaperones interfere with the formation of scrapie prion protein. EMBO J 15: 6363-6373.
62. Ulloa-Aguirre A, Janovick JA, Brothers SP, Conn PM (2004) Pharmacologic rescue of conformationally-defective proteins: Implications for the treatment of human disease. Traffic 5: 821-837.
63. Varga K, Jurkuvenaite A, Wakefield J, et al (2004) Efficient intracellular processing of the endogenous cystic fibrosis transmembrane conductance regulator in epithelial cell lines. J Biol Chem 279: 22578-22584.
64. Verkman AS (2004) Drug discovery in academia. Am J Physiol Cell Physiol 286: C465-C474.
65. Wang SM, Khandekar JD, Kaul KL, Winchester DJ, Morimoto RI (1999) A method for the quantitative analysis of human heat shock gene expression using a multiplex RT-PCR assay. Cell Stress Chaperones 4: 153-161.
66. Ward CL, Omura S, Kopito RR (1995) Degradation of CFTR by the ubiquitin-proteasome pathway. Cell 83: 121-127.
67. Wegele H, Muller L, Buchner J (2004) Hsp70 and Hsp90-a relay team for protein folding. Rev Physiol Biochem Pharmacol 151: 1-44.
68. Welch WJ (2004) Role of quality control pathways in human diseases involving protein misfolding. Semin Cell Dev Biol 15: 31-38.
69. Welch WJ, Brown CR (1996) Influence of molecular and chemical chaperones on protein folding. Cell Stress Chaperones 1: 109-115.
70. Welsh MJ, Tsui L-C, Boat TF, Beaudet AL (1996) Cystic fibrosis. In: Scriver CR, Beaudet AL, Sly WS, Valle D, eds; Childs B, Kinzler KW, Vogelstein B, assoc, eds. The Metabolic and Molecular Bases of Inherited Disease, 8th edn. New York: McGraw-Hill, 3799-3876.
71. Westerheide SD, Bosman JD, Mbadugha BN, et al (2004) Celastrols as inducers of the heat shock response and cytoprotection. J Biol Chem 279: 56053-56060.
72. Whitesell L, Lindquist SL (2005) HSP90 and the chaperoning of cancer. Nat Rev Cancer 5: 761-772.
73. Yang Y, Janich S, Cohn JA, Wilson JM (1993) The common variant of cystic fibrosis transmembrane conductance regulator is recognized by hsp70 and degraded in a pre-Golgi nonlysosomal compartment. Proc Natl Acad Sci USA 90: 9480-9484.
74. Zhang XM, Wang XT, Yue H, et al (2003a) Organic solutes rescue the functional defect in delta F508 cystic fibrosis transmembrane conductance regulator. J Biol Chem 278: 51232-51242.
75. Zhang Z, Ferraris JD, Brooks HL, Brisc I, Burg MB (2003b) Expression of osmotic stress-related genes in tissues of normal and hyposmotic rats. Am J Physiol Renal Physiol 285: F688-F693.
76. Younger JM, Ren HY, Chen L, Fan CY, Fields A, Patterson C, Cyr DM (2004) A foldable CFTR (Delta) 7508 biogenic intermediate accummulates upon inhibition of the Hsc70-CHIP E3 ubiquitin ligase. J Cell Biol 167: 1075-1085.